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Aspartate--tRNA ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS)

 SYD_MYCGE               Reviewed;         550 AA.
P47282; Q49462; Q49479;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044};
EC=6.1.1.12 {ECO:0000255|HAMAP-Rule:MF_00044};
AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=MG036;
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=243273;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33530 / G-37 / NCTC 10195;
PubMed=7569993; DOI=10.1126/science.270.5235.397;
Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
"The minimal gene complement of Mycoplasma genitalium.";
Science 270:397-403(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-550.
STRAIN=ATCC 33530 / G-37 / NCTC 10195;
PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
"A survey of the Mycoplasma genitalium genome by using random
sequencing.";
J. Bacteriol. 175:7918-7930(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-470.
STRAIN=ATCC 33530 / G-37 / NCTC 10195;
PubMed=1945886; DOI=10.1093/nar/19.21.6027;
Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
"A random sequencing approach for placing markers on the physical map
of Mycoplasma genitalium.";
Nucleic Acids Res. 19:6027-6031(1991).
-!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in
a two-step reaction: L-aspartate is first activated by ATP to form
Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
{ECO:0000255|HAMAP-Rule:MF_00044}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
diphosphate + L-aspartyl-tRNA(Asp). {ECO:0000255|HAMAP-
Rule:MF_00044}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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EMBL; L43967; AAC71252.1; -; Genomic_DNA.
EMBL; U01814; AAD12351.1; -; Genomic_DNA.
EMBL; X61523; CAA43736.1; -; Genomic_DNA.
PIR; I64203; I64203.
ProteinModelPortal; P47282; -.
SMR; P47282; -.
STRING; 243273.MgenG_010200001005; -.
EnsemblBacteria; AAC71252; AAC71252; MG_036.
KEGG; mge:MG_036; -.
eggNOG; ENOG4105C9M; Bacteria.
eggNOG; COG0173; LUCA.
KO; K01876; -.
OMA; YQLDVEM; -.
OrthoDB; POG091H021G; -.
Proteomes; UP000000807; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
InterPro; IPR004364; aa-tRNA-synt_II.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004524; Asp-tRNA-ligase_1.
InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
InterPro; IPR004115; GAD-like.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
Pfam; PF00152; tRNA-synt_2; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PRINTS; PR01042; TRNASYNTHASP.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF55261; SSF55261; 1.
TIGRFAMs; TIGR00459; aspS_bact; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
CHAIN 1 550 Aspartate--tRNA ligase.
/FTId=PRO_0000110902.
NP_BIND 208 210 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
NP_BIND 499 502 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
REGION 186 189 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 162 162 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 208 208 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 217 217 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
BINDING 417 417 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
BINDING 451 451 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}.
BINDING 458 458 Aspartate. {ECO:0000255|HAMAP-
Rule:MF_00044}.
CONFLICT 374 377 LGAI -> CWSN (in Ref. 2; AAD12351).
{ECO:0000305}.
CONFLICT 469 470 MN -> II (in Ref. 3; CAA43736).
{ECO:0000305}.
SEQUENCE 550 AA; 64237 MW; 4B7972691E38D4BA CRC64;
MCFNQRILIG SISTEQLNKT IVIIGWIKRI KKLGEINFII VGDKSGTIQV TCKDKEQIQQ
LTREDIVIVK AKLQRLDSVR FELINPTIKL FSKSKTPPLI IEDETDALEE VRLKYRYLDL
RRRLMQKRLL LRHQFILAIR NWFNQQGFIE IETPTLSKST PEGAQDFLVP ARIRKDCFYA
LVQSPQIYKQ LLMIAGVEKY FQIARVYRDE DSRKDRQPEH TQIDFEISFC NQKMIMNLVE
KLFFSVFLDV FQIKIKKTFP VFKFSELFER FGSDKPDLRY GFEIKDFTSL FQDHQNQFTK
LIEAKGIIGG IELTNIELST DKIKALRKIA KDHDVSLEVH NKNNSTLKTS IKCDEKNTLL
LVANKSKKKA WTALGAIRNE LKYHLDIVKP NQYSFCWVVD FPLYDFDEKT NQWISNHNIF
SKPKQEWIDN FESNKNEALS EQFDLVLNGF EIGSGSIRIN DPIVQKRLMN SLNIDPNKFA
FLLEAYQYGA PVHGGMGLGI DRLMMILNQT DNIREVIAFP KNNHGIEVHT NAPDKIDKEE
VKWWIKELVK


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